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==Crystal Structure of CalO1, Methyltransferase in Calicheamicin Biosynthesis, SAH bound form==
==Crystal Structure of CalO1, Methyltransferase in Calicheamicin Biosynthesis, SAH bound form==
<StructureSection load='3lst' size='340' side='right' caption='[[3lst]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='3lst' size='340' side='right'caption='[[3lst]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3lst]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_15837 Atcc 15837]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LST OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LST FirstGlance]. <br>
<table><tr><td colspan='2'>[[3lst]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Micromonospora_echinospora Micromonospora echinospora]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LST OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LST FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">calO1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1877 ATCC 15837])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3lst FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lst OCA], [https://pdbe.org/3lst PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lst RCSB], [https://www.ebi.ac.uk/pdbsum/3lst PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lst ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lst FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lst OCA], [http://pdbe.org/3lst PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lst RCSB], [http://www.ebi.ac.uk/pdbsum/3lst PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lst ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8KNE5_MICEC Q8KNE5_MICEC]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ls/3lst_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ls/3lst_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 15837]]
[[Category: Large Structures]]
[[Category: Bingman, C A]]
[[Category: Micromonospora echinospora]]
[[Category: Structural genomic]]
[[Category: Bingman CA]]
[[Category: Chang, A]]
[[Category: Chang A]]
[[Category: Phillips, G N]]
[[Category: Phillips Jr GN]]
[[Category: Singh, S]]
[[Category: Singh S]]
[[Category: Thorson, J S]]
[[Category: Thorson JS]]
[[Category: Calicheamicin]]
[[Category: Calo1]]
[[Category: Cesg]]
[[Category: Enediyne]]
[[Category: Methyltransferase]]
[[Category: PSI, Protein structure initiative]]
[[Category: Sah]]
[[Category: Transferase]]

Latest revision as of 08:58, 17 October 2024

Crystal Structure of CalO1, Methyltransferase in Calicheamicin Biosynthesis, SAH bound formCrystal Structure of CalO1, Methyltransferase in Calicheamicin Biosynthesis, SAH bound form

Structural highlights

3lst is a 2 chain structure with sequence from Micromonospora echinospora. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8KNE5_MICEC

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The X-ray structure determination at 2.4 A resolution of the putative orsellinic acid C3 O-methyltransferase (CalO1) involved in calicheamicin biosynthesis is reported. Comparison of CalO1 with a homology model of the functionally related calicheamicin orsellinic acid C2 O-methyltransferase (CalO6) implicates several residues that are likely to contribute to the regiospecificity of alkylation. Consistent with the proposed requirement of an acyl-carrier-protein-bound substrate, this structural study also reveals structural determinants within CalO1 that are anticipated to accommodate an association with an acyl carrier protein.

Structural characterization of CalO1: a putative orsellinic acid methyltransferase in the calicheamicin-biosynthetic pathway.,Chang A, Singh S, Bingman CA, Thorson JS, Phillips GN Jr Acta Crystallogr D Biol Crystallogr. 2011 Mar;67(Pt 3):197-203. Epub 2011, Feb 15. PMID:21358050[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Chang A, Singh S, Bingman CA, Thorson JS, Phillips GN Jr. Structural characterization of CalO1: a putative orsellinic acid methyltransferase in the calicheamicin-biosynthetic pathway. Acta Crystallogr D Biol Crystallogr. 2011 Mar;67(Pt 3):197-203. Epub 2011, Feb 15. PMID:21358050 doi:10.1107/S090744491100360X

3lst, resolution 2.40Å

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OCA
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